AUP1_HUMAN
ID AUP1_HUMAN Reviewed; 410 AA.
AC Q9Y679; C0H5W8; Q9H866; Q9UNQ6; Q9Y685;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Lipid droplet-regulating VLDL assembly factor AUP1 {ECO:0000312|HGNC:HGNC:891};
DE AltName: Full=Ancient ubiquitous protein 1 {ECO:0000303|PubMed:12042322};
GN Name=AUP1 {ECO:0000312|HGNC:HGNC:891};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Pituitary;
RA Peng Y., Song H., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G.,
RA Luo M., Chen J., Hu R.;
RT "Human ancient ubiquitous protein AUP1 isoform gene.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hematopoietic stem cell;
RA Gu J., Huang Q., Yu Y., Xu S., Han Z., Fu G., Zhou J., Wang Y., Huang C.,
RA Ren S., Tu Y., Chen Z.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT myelodysplastic syndrome patients.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP SUBCELLULAR LOCATION, INTERACTION WITH ITGA2B; ITGA1; ITGA2; ITGA5; ITGAV
RP AND ITGAM, AND TISSUE SPECIFICITY.
RX PubMed=12042322; DOI=10.1074/jbc.m204340200;
RA Kato A., Kawamata N., Tamayose K., Egashira M., Miura R., Fujimura T.,
RA Murayama K., Oshimi K.;
RT "Ancient ubiquitous protein 1 binds to the conserved membrane-proximal
RT sequence of the cytoplasmic tail of the integrin alpha subunits that plays
RT a crucial role in the inside-out signaling of alpha IIbbeta 3.";
RL J. Biol. Chem. 277:28934-28941(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288 AND THR-367, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-292; SER-363 AND
RP THR-367, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION IN A COMPLEX WITH SEL1L, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18711132; DOI=10.1073/pnas.0805371105;
RA Mueller B., Klemm E.J., Spooner E., Claessen J.H., Ploegh H.L.;
RT "SEL1L nucleates a protein complex required for dislocation of misfolded
RT glycoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12325-12330(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP FUNCTION, INTERACTION WITH UBE2G2, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP MUTAGENESIS OF 397-ALA--THR-402.
RX PubMed=21127063; DOI=10.1074/jbc.m110.190785;
RA Spandl J., Lohmann D., Kuerschner L., Moessinger C., Thiele C.;
RT "Ancient ubiquitous protein 1 (AUP1) localizes to lipid droplets and binds
RT the E2 ubiquitin conjugase G2 (Ube2g2) via its G2 binding region.";
RL J. Biol. Chem. 286:5599-5606(2011).
RN [15]
RP FUNCTION, INTERACTION WITH UBE2G2, SUBCELLULAR LOCATION, DOMAIN,
RP UBIQUITINATION, AND MUTAGENESIS OF HIS-96; 306-GLU--LEU-308 AND
RP 333-LEU-LEU-334.
RX PubMed=21857022; DOI=10.1074/jbc.m111.284794;
RA Klemm E.J., Spooner E., Ploegh H.L.;
RT "Dual role of ancient ubiquitous protein 1 (AUP1) in lipid droplet
RT accumulation and endoplasmic reticulum (ER) protein quality control.";
RL J. Biol. Chem. 286:37602-37614(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF 33-PRO--GLY-35; ARG-42;
RP ASP-58 AND 62-ARG-ARG-63.
RX PubMed=23197321; DOI=10.1194/jlr.m033852;
RA Stevanovic A., Thiele C.;
RT "Monotopic topology is required for lipid droplet targeting of ancient
RT ubiquitous protein 1.";
RL J. Lipid Res. 54:503-513(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-288 AND THR-367, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP FUNCTION, INTERACTION WITH AMFR; RNF139 AND UBE2G2, SUBCELLULAR LOCATION,
RP DOMAIN, AND MUTAGENESIS OF ARG-382; GLN-383; GLU-384; LEU-386; GLU-388;
RP ARG-389; LYS-390; LEU-393; ARG-398; ARG-399; ARG-400; ARG-404; GLU-408 AND
RP ASP-410.
RX PubMed=23223569; DOI=10.1091/mbc.e12-07-0564;
RA Jo Y., Hartman I.Z., DeBose-Boyd R.A.;
RT "Ancient ubiquitous protein-1 mediates sterol-induced ubiquitination of 3-
RT hydroxy-3-methylglutaryl CoA reductase in lipid droplet-associated
RT endoplasmic reticulum membranes.";
RL Mol. Biol. Cell 24:169-183(2013).
RN [21]
RP FUNCTION, DOMAIN, UBIQUITINATION, AND MUTAGENESIS OF 33-PRO--GLY-35;
RP 307-VAL--PRO-309; ILE-316; 319-ASP-LEU-320; 329-THR-ILE-330 AND
RP 333-LEU-LEU-334.
RX PubMed=24039768; DOI=10.1371/journal.pone.0072453;
RA Lohmann D., Spandl J., Stevanovic A., Schoene M., Philippou-Massier J.,
RA Thiele C.;
RT "Monoubiquitination of ancient ubiquitous protein 1 promotes lipid droplet
RT clustering.";
RL PLoS ONE 8:e72453-e72453(2013).
RN [22]
RP FUNCTION, INTERACTION WITH APOB, AND SUBCELLULAR LOCATION.
RX PubMed=28183703; DOI=10.1161/atvbaha.117.309000;
RA Zhang J., Zamani M., Thiele C., Taher J., Amir Alipour M., Yao Z.,
RA Adeli K.;
RT "AUP1 (Ancient Ubiquitous Protein 1) Is a Key Determinant of Hepatic Very-
RT Low-Density Lipoprotein Assembly and Secretion.";
RL Arterioscler. Thromb. Vasc. Biol. 37:633-642(2017).
RN [23]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH DENV NS4A, SUBCELLULAR
RP LOCATION, INDUCTION (MICROBIAL INFECTION), UBIQUITINATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29902443; DOI=10.1016/j.chom.2018.05.005;
RA Zhang J., Lan Y., Li M.Y., Lamers M.M., Fusade-Boyer M., Klemm E.,
RA Thiele C., Ashour J., Sanyal S.;
RT "Flaviviruses Exploit the Lipid Droplet Protein AUP1 to Trigger Lipophagy
RT and Drive Virus Production.";
RL Cell Host Microbe 23:819-831.e5(2018).
RN [24]
RP STRUCTURE BY NMR OF 292-345.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-075, a human CUE domain.";
RL Submitted (SEP-2007) to the PDB data bank.
CC -!- FUNCTION: Plays a role in the translocation of terminally misfolded
CC proteins from the endoplasmic reticulum lumen to the cytoplasm and
CC their degradation by the proteasome (PubMed:18711132, PubMed:21857022).
CC Plays a role in lipid droplet formation (PubMed:21857022). Induces
CC lipid droplet clustering (PubMed:24039768). Recruits ubiquitin-
CC conjugating enzyme UBE2G2 to lipid droplets which facilitates its
CC interaction with ubiquitin ligases AMFR/gp78 and RNF139/TRC8, leading
CC to sterol-induced ubiquitination of HMGCR and its subsequent
CC proteasomal degradation (PubMed:23223569, PubMed:21127063). Also
CC required for the degradation of INSIG1, SREBF1 and SREBF2
CC (PubMed:23223569). Plays a role in regulating assembly and secretion of
CC very low density lipoprotein particles and stability of apolipoprotein
CC APOB (PubMed:28183703). {ECO:0000269|PubMed:18711132,
CC ECO:0000269|PubMed:21127063, ECO:0000269|PubMed:21857022,
CC ECO:0000269|PubMed:23223569, ECO:0000269|PubMed:24039768,
CC ECO:0000269|PubMed:28183703}.
CC -!- FUNCTION: (Microbial infection) Following Dengue virus infection,
CC required for induction of lipophagy which facilitates production of
CC virus progeny particles. {ECO:0000269|PubMed:29902443}.
CC -!- SUBUNIT: Identified in a complex that contains SEL1L, OS9, FAF2/UBXD8,
CC UBE2J1/UBC6E and AUP1 (PubMed:18711132). Interacts with the cytoplasmic
CC tail of ITGA2B, ITGA1, ITGA2, ITGA5, ITGAV and ITGAM (PubMed:12042322).
CC Interacts (via C-terminus) with ubiquitin-conjugating enzyme UBE2G2;
CC the interaction recruits UBE2G2 to lipid droplets (PubMed:21127063,
CC PubMed:23223569). Interacts with ubiquitin ligases AMFR/gp78 and
CC RNF139/TRC8; this promotes interaction of UBE2G2 with AMFR and RNF139
CC (PubMed:23223569). Interacts with apolipoprotein APOB
CC (PubMed:28183703). {ECO:0000269|PubMed:12042322,
CC ECO:0000269|PubMed:18711132, ECO:0000269|PubMed:21127063,
CC ECO:0000269|PubMed:23223569, ECO:0000269|PubMed:28183703}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Dengue virus NS4A; the
CC interaction occurs in the presence of Dengue virus NS4B and induces
CC lipophagy which facilitates production of virus progeny.
CC {ECO:0000269|PubMed:29902443}.
CC -!- INTERACTION:
CC Q9Y679; P35372: OPRM1; NbExp=4; IntAct=EBI-1058701, EBI-2624570;
CC Q9Y679; P60604: UBE2G2; NbExp=6; IntAct=EBI-1058701, EBI-1051028;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12042322, ECO:0000269|PubMed:18711132,
CC ECO:0000269|PubMed:21127063, ECO:0000269|PubMed:21857022,
CC ECO:0000269|PubMed:23197321, ECO:0000269|PubMed:23223569}; Peripheral
CC membrane protein {ECO:0000269|PubMed:21127063,
CC ECO:0000269|PubMed:23197321}. Lipid droplet
CC {ECO:0000269|PubMed:21127063, ECO:0000269|PubMed:21857022,
CC ECO:0000269|PubMed:23197321, ECO:0000269|PubMed:23223569,
CC ECO:0000269|PubMed:28183703, ECO:0000269|PubMed:29902443}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
CC {ECO:0000269|PubMed:29902443}. Note=(Microbial infection) Upon Dengue
CC virus infection, relocates from lipid droplets to autophagosomes.
CC {ECO:0000269|PubMed:29902443}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y679-2; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y679-3; Sequence=VSP_059683, VSP_059684;
CC -!- TISSUE SPECIFICITY: Detected in blood platelets and leukocytes (at
CC protein level). Ubiquitous. Highly expressed in placenta, liver,
CC kidney, skeletal muscle, heart and brain.
CC {ECO:0000269|PubMed:12042322}.
CC -!- INDUCTION: (Microbial infection) By Dengue virus infection (at protein
CC level). {ECO:0000269|PubMed:29902443}.
CC -!- DOMAIN: The CUE domain is required for interaction with the ER quality
CC control machinery and misfolded substrates, ubiquitination, lipid
CC clustering and interaction with AMFR but is not required for
CC localization to lipid droplets. {ECO:0000269|PubMed:21857022,
CC ECO:0000269|PubMed:23223569, ECO:0000269|PubMed:24039768}.
CC -!- PTM: Monoubiquitinated and diubiquitinated.
CC {ECO:0000269|PubMed:21857022, ECO:0000269|PubMed:24039768,
CC ECO:0000269|PubMed:29902443}.
CC -!- PTM: (Microbial infection) Not ubiquitinated following Dengue virus
CC infection. {ECO:0000269|PubMed:29902443}.
CC -!- SIMILARITY: Belongs to the AUP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD43018.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH33646.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF100754; AAD43018.1; ALT_FRAME; mRNA.
DR EMBL; AF100753; AAD43017.1; -; mRNA.
DR EMBL; AF100746; AAD43010.1; -; mRNA.
DR EMBL; AF165515; AAF86645.1; -; mRNA.
DR EMBL; AK023983; BAB14753.1; -; mRNA.
DR EMBL; CH471053; EAW99623.1; -; Genomic_DNA.
DR EMBL; BC001658; AAH01658.1; -; mRNA.
DR EMBL; BC033646; AAH33646.2; ALT_INIT; mRNA.
DR CCDS; CCDS42702.1; -. [Q9Y679-2]
DR RefSeq; NP_853553.1; NM_181575.4. [Q9Y679-2]
DR PDB; 2EKF; NMR; -; A=292-345.
DR PDB; 7LEW; X-ray; 1.74 A; B=379-410.
DR PDBsum; 2EKF; -.
DR PDBsum; 7LEW; -.
DR AlphaFoldDB; Q9Y679; -.
DR SMR; Q9Y679; -.
DR BioGRID; 107031; 249.
DR CORUM; Q9Y679; -.
DR IntAct; Q9Y679; 58.
DR MINT; Q9Y679; -.
DR STRING; 9606.ENSP00000366748; -.
DR iPTMnet; Q9Y679; -.
DR PhosphoSitePlus; Q9Y679; -.
DR SwissPalm; Q9Y679; -.
DR BioMuta; AUP1; -.
DR DMDM; 12643958; -.
DR EPD; Q9Y679; -.
DR jPOST; Q9Y679; -.
DR MassIVE; Q9Y679; -.
DR MaxQB; Q9Y679; -.
DR PaxDb; Q9Y679; -.
DR PeptideAtlas; Q9Y679; -.
DR PRIDE; Q9Y679; -.
DR ProteomicsDB; 86617; -. [Q9Y679-2]
DR ProteomicsDB; 86618; -. [Q9Y679-3]
DR Antibodypedia; 2357; 198 antibodies from 27 providers.
DR DNASU; 550; -.
DR Ensembl; ENST00000377526.4; ENSP00000366748.3; ENSG00000115307.17. [Q9Y679-2]
DR Ensembl; ENST00000425118.5; ENSP00000403430.1; ENSG00000115307.17. [Q9Y679-3]
DR GeneID; 550; -.
DR KEGG; hsa:550; -.
DR MANE-Select; ENST00000377526.4; ENSP00000366748.3; NM_181575.5; NP_853553.1.
DR UCSC; uc002smf.4; human. [Q9Y679-2]
DR CTD; 550; -.
DR DisGeNET; 550; -.
DR GeneCards; AUP1; -.
DR HGNC; HGNC:891; AUP1.
DR HPA; ENSG00000115307; Low tissue specificity.
DR MIM; 602434; gene.
DR neXtProt; NX_Q9Y679; -.
DR OpenTargets; ENSG00000115307; -.
DR PharmGKB; PA25182; -.
DR VEuPathDB; HostDB:ENSG00000115307; -.
DR GeneTree; ENSGT00390000016110; -.
DR HOGENOM; CLU_045696_0_0_1; -.
DR InParanoid; Q9Y679; -.
DR OMA; CLMLIRI; -.
DR OrthoDB; 1319689at2759; -.
DR PhylomeDB; Q9Y679; -.
DR TreeFam; TF313372; -.
DR PathwayCommons; Q9Y679; -.
DR SignaLink; Q9Y679; -.
DR BioGRID-ORCS; 550; 59 hits in 1084 CRISPR screens.
DR ChiTaRS; AUP1; human.
DR EvolutionaryTrace; Q9Y679; -.
DR GeneWiki; AUP1; -.
DR GenomeRNAi; 550; -.
DR Pharos; Q9Y679; Tbio.
DR PRO; PR:Q9Y679; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9Y679; protein.
DR Bgee; ENSG00000115307; Expressed in granulocyte and 198 other tissues.
DR Genevisible; Q9Y679; HS.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IBA:GO_Central.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IMP:UniProtKB.
DR GO; GO:0140042; P:lipid droplet formation; IMP:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; IDA:UniProtKB.
DR GO; GO:0061724; P:lipophagy; IMP:UniProtKB.
DR GO; GO:1990044; P:protein localization to lipid droplet; IDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; IMP:UniProtKB.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB.
DR InterPro; IPR003892; CUE.
DR Pfam; PF02845; CUE; 1.
DR SMART; SM00546; CUE; 1.
DR PROSITE; PS51140; CUE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Host-virus interaction; Lipid droplet; Membrane;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..410
FT /note="Lipid droplet-regulating VLDL assembly factor AUP1"
FT /id="PRO_0000020765"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21127063,
FT ECO:0000305|PubMed:23197321"
FT INTRAMEM 21..41
FT /evidence="ECO:0000305|PubMed:21127063,
FT ECO:0000305|PubMed:23197321"
FT TOPO_DOM 42..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:21127063,
FT ECO:0000305|PubMed:23197321"
FT DOMAIN 296..338
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 255..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 367
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 360..373
FT /note="FPSSGPVTPQPTAL -> AFDACLMMMTPQAL (in isoform 2)"
FT /id="VSP_059683"
FT VAR_SEQ 374..410
FT /note="Missing (in isoform 2)"
FT /id="VSP_059684"
FT MUTAGEN 33..35
FT /note="PVG->LLL: Disrupts topology with the N-terminus in
FT the lumen instead of the cytoplasm. Abolishes lipid droplet
FT localization and lipid droplet clustering."
FT /evidence="ECO:0000269|PubMed:23197321,
FT ECO:0000269|PubMed:24039768"
FT MUTAGEN 42
FT /note="R->I: Abolishes lipid droplet localization."
FT /evidence="ECO:0000269|PubMed:23197321"
FT MUTAGEN 58
FT /note="D->I: Does not affect lipid droplet localization."
FT /evidence="ECO:0000269|PubMed:23197321"
FT MUTAGEN 62..63
FT /note="RR->FF: Abolishes lipid droplet localization."
FT /evidence="ECO:0000269|PubMed:23197321"
FT MUTAGEN 96
FT /note="H->A: Reduced formation of lipid droplets."
FT /evidence="ECO:0000269|PubMed:21857022"
FT MUTAGEN 306..308
FT /note="EVL->KAA: Reduced interaction with ER quality
FT control machinery and misfolded substrates; when associated
FT with 333-L-L-334 Del."
FT /evidence="ECO:0000269|PubMed:21857022"
FT MUTAGEN 307..309
FT /note="VLP->GGR: Reduced lipid droplet clustering."
FT /evidence="ECO:0000269|PubMed:24039768"
FT MUTAGEN 316
FT /note="I->R: Reduced lipid droplet clustering; when
FT associated with 319-V-E-320 and 333-E-D-334."
FT /evidence="ECO:0000269|PubMed:24039768"
FT MUTAGEN 319..320
FT /note="DL->VE: Reduced lipid droplet clustering; when
FT associated with R-316 and 333-E-D-334."
FT /evidence="ECO:0000269|PubMed:24039768"
FT MUTAGEN 329..330
FT /note="TI->AD: Reduced lipid droplet clustering."
FT /evidence="ECO:0000269|PubMed:24039768"
FT MUTAGEN 333..334
FT /note="LL->ED: Reduced lipid droplet clustering; when
FT associated with R-316 and 319-V-E-320."
FT /evidence="ECO:0000269|PubMed:24039768"
FT MUTAGEN 333..334
FT /note="Missing: Reduced interaction with ER quality control
FT machinery and misfolded substrates; when associated with
FT 306-K--A-308."
FT /evidence="ECO:0000269|PubMed:21857022"
FT MUTAGEN 382
FT /note="R->A: Significantly reduced interaction with
FT UBE2G2."
FT /evidence="ECO:0000269|PubMed:23223569"
FT MUTAGEN 383
FT /note="Q->A: Significantly reduced interaction with
FT UBE2G2."
FT /evidence="ECO:0000269|PubMed:23223569"
FT MUTAGEN 384
FT /note="E->A: No effect on interaction with UBE2G2."
FT /evidence="ECO:0000269|PubMed:23223569"
FT MUTAGEN 386
FT /note="L->A: Abolishes interaction with UBE2G2."
FT /evidence="ECO:0000269|PubMed:23223569"
FT MUTAGEN 388
FT /note="E->A: No effect on interaction with UBE2G2."
FT /evidence="ECO:0000269|PubMed:23223569"
FT MUTAGEN 389
FT /note="R->A: Significantly reduced interaction with
FT UBE2G2."
FT /evidence="ECO:0000269|PubMed:23223569"
FT MUTAGEN 390
FT /note="K->A: Abolishes interaction with UBE2G2."
FT /evidence="ECO:0000269|PubMed:23223569"
FT MUTAGEN 393
FT /note="L->A: Abolishes interaction with UBE2G2."
FT /evidence="ECO:0000269|PubMed:23223569"
FT MUTAGEN 397..402
FT /note="ARRRFT->EGREDA: Abolishes interaction with UBE2G2."
FT /evidence="ECO:0000269|PubMed:21127063"
FT MUTAGEN 398
FT /note="R->A: Significantly reduced interaction with
FT UBE2G2."
FT /evidence="ECO:0000269|PubMed:23223569"
FT MUTAGEN 399
FT /note="R->A: No effect on interaction with UBE2G2."
FT /evidence="ECO:0000269|PubMed:23223569"
FT MUTAGEN 400
FT /note="R->A: Abolishes interaction with UBE2G2."
FT /evidence="ECO:0000269|PubMed:23223569"
FT MUTAGEN 404
FT /note="R->A: Abolishes interaction with UBE2G2."
FT /evidence="ECO:0000269|PubMed:23223569"
FT MUTAGEN 408
FT /note="E->A: Significantly reduced interaction with
FT UBE2G2."
FT /evidence="ECO:0000269|PubMed:23223569"
FT MUTAGEN 410
FT /note="D->A: No effect on interaction with UBE2G2."
FT /evidence="ECO:0000269|PubMed:23223569"
FT CONFLICT 288
FT /note="S -> P (in Ref. 3; AAD43010)"
FT /evidence="ECO:0000305"
FT HELIX 297..307
FT /evidence="ECO:0007829|PDB:2EKF"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:2EKF"
FT HELIX 313..321
FT /evidence="ECO:0007829|PDB:2EKF"
FT HELIX 326..334
FT /evidence="ECO:0007829|PDB:2EKF"
FT HELIX 379..402
FT /evidence="ECO:0007829|PDB:7LEW"
SQ SEQUENCE 410 AA; 45787 MW; 1A06476225C5DFDC CRC64;
MELPSGPGPE RLFDSHRLPG DCFLLLVLLL YAPVGFCLLV LRLFLGIHVF LVSCALPDSV
LRRFVVRTMC AVLGLVARQE DSGLRDHSVR VLISNHVTPF DHNIVNLLTT CSTPLLNSPP
SFVCWSRGFM EMNGRGELVE SLKRFCASTR LPPTPLLLFP EEEATNGREG LLRFSSWPFS
IQDVVQPLTL QVQRPLVSVT VSDASWVSEL LWSLFVPFTV YQVRWLRPVH RQLGEANEEF
ALRVQQLVAK ELGQTGTRLT PADKAEHMKR QRHPRLRPQS AQSSFPPSPG PSPDVQLATL
AQRVKEVLPH VPLGVIQRDL AKTGCVDLTI TNLLEGAVAF MPEDITKGTQ SLPTASASKF
PSSGPVTPQP TALTFAKSSW ARQESLQERK QALYEYARRR FTERRAQEAD
